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Human PFKFB3 in complex with a N-aryl 6-aminoquinoxaline inhibitor 4

Analyse Human PFKFB3 in complex with a N-aryl 6-aminoquinoxaline inhibitor 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6IC0
Type
protein
Length
428 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
UniProt
Q16875
Ligands
HAK, POP, F6P

Structure

x-ray diffraction · 1 distinct chain.

ChainMoleculeTypeResiduesSecondary structureUniProt
A—protein428—Q16875

Ligands and binding sites

  • HAK · 3-[[8-(1-methylindol-6-yl)quinoxalin-6-yl]amino]-~{N}-pyrimidin-5-yl-pyridine-4-carboxamide · ligand · chains A
  • POP · Pyrophosphate 2- · ligand · chains A
  • F6P · 6-O-phosphono-beta-D-fructofuranose · ligand · chains A
  • FLC · Citrate anion · additive · chains A
  • DMS · Dimethyl sulfoxide · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

  • 6IC0 · Human PFKFB3 in complex with a N-Aryl 6-Aminoquinoxaline inhibitor 4 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q16875 · AlphaFold monomer V2.0 prediction for 6-phosphofructo-2-KINASE/FRUCTOSE-2,6-bisphosphatase… · a predicted model of the same protein · chain A against A, TM-score 0.99

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